Výsledky vyhledávání - "Stephan, Kiessling"

BCL-2 Modifying Factor (BMF) Is a Central Regulator of Anoikis in Human Intestinal Epithelial Cells

Autor: Helen M. Becker, Claudia Hofmann, Christian Ploner, Stephan Kiessling, Florian Obermeier, Martin Hausmann, Katharina Leucht, Andreas Villunger, Michael Fried, Gerhard Rogler, Michaela Krebs, Jürgen Schölmerich, Silvia Kellermeier, Werner Falk

Publikováno v: Journal of Biological Chemistry. 286:26533-26540

BCL-2 modifying factor (BMF) is a sentinel considered to register damage at the cytoskeleton and to convey a death signal to B-cell lymphoma 2. B-cell lymphoma 2 is neutralized by BMF and thereby facilitates cytochrome C release from mitochondria. We

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef5ea5c184e1a6f13b22ba4aabcc09fe
https://doi.org/10.1074/jbc.m111.265322

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Loss of the BH3-only protein Bmf impairs B cell homeostasis and accelerates γ irradiation–induced thymic lymphoma development

Autor: Andreas Strasser, Claudia Manzl, Anna Frenzel, Stephan Kiessling, Miriam Erlacher, Verena Labi, Andreas Villunger, Lorraine A. O'Reilly

Publikováno v: The Journal of Experimental Medicine

Members of the Bcl-2 protein family play crucial roles in the maintenance of tissue homeostasis by regulating apoptosis in response to developmental cues or exogenous stress. Proapoptotic BH3-only members of the Bcl-2 family are essential for initiat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe3744890690673bc27bef8c161f86cf
https://doi.org/10.1084/jem.20071658

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BH3-only proteins in cell death initiation, malignant disease and anticancer therapy

Autor: Stephan Kiessling, Verena Labi, Andreas Villunger, Miriam Erlacher

Publikováno v: Cell Death & Differentiation. 13:1325-1338

Induction of apoptosis in tumour cells, either by direct activation of the death receptor pathway using agonistic antibodies or recombinant ligands, or direct triggering of the Bcl-2-regulated intrinsic apoptosis pathway by small molecule drugs, carr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a669338348952bba27543bbdc0d481e9
https://doi.org/10.1038/sj.cdd.4401940

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Functional expression of the interleukin-11 receptor alpha-chain in normal colonic epithelium and colon cancer

Autor: Hans H Herfarth, Martin Hausmann, Gerhard Müller-Newen, Stephan Kiessling, Gerhard Rogler, Frauke Bataille, Jürgen Schölmerich, Peter C. Heinrich, Nicole Deutscher, Sandra N. Leeb

Publikováno v: International Journal of Colorectal Disease. 21:573-581

Interleukin-11 (IL-11) has been evaluated as an anti-inflammatory and mucosa-protective therapeutic agent in inflammatory bowel diseases (IBDs). Activity of IL-11 requires binding to the alpha receptor subunit (IL-11Ralpha) that provides ligand speci

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e39641da8abf3a554aa3a807b214434
https://doi.org/10.1007/s00384-005-0055-8

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Functional Expression of the Interleukin-11 Receptor α-Chain and Evidence of Antiapoptotic Effects in Human Colonic Epithelial Cells

Autor: Gerhard Müller-Newen, Peter C. Heinrich, Johannes Grossmann, Armin Buschauer, Stephan Kiessling, Martin Hausmann, Jörn Sträter, Jürgen Schölmerich, Felix A. Montero-Julian, Heiko C. Rath, Sandra N. Leeb, Klaus Schlottmann, T. Andus, Gerhard Rogler, T. Spöttl

Publikováno v: Journal of Biological Chemistry. 279:10304-10315

A tissue-protective effect of interleukin-11 (IL-11) for the intestinal mucosa has been postulated from animal models of inflammatory bowel disease (IBD). Despite the fact that the clinical usefulness of the anti-inflammatory effects of this cytokine

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d299fc56a379fb7caf70edf6a5b850a8
https://doi.org/10.1074/jbc.m312757200

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Fas-associated death domain protein interacts with methyl-CpG binding domain protein 4: A potential link between genome surveillance and apoptosis

Autor: Adrian Bird, Owen J. Sansom, Stephan Kiessling, Kathryn Maddison, Robert A. Screaton, Catherine B. Millar, Steven M. Frisch, Alan Richard Clarke

Publikováno v: Proceedings of the National Academy of Sciences. 100:5211-5216

Fas-associated death domain protein (FADD) is an adaptor protein bridging death receptors with initiator caspases. Thus, its function and localization are assumed to be cytoplasmic, although the localization of endogenous FADD has not been reported.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::929ce08f2707e28ea9730d6fc116ef2a
https://doi.org/10.1073/pnas.0431215100

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